An immunofluorescence study of extracellular matrix associated with cytotrophoblast of the chorion laeve

Abstract

Using immunofluorescence we have studied the distribution within and beneath the cytotrophoblast of chorion laeve of five extracellular matrix components: types I, III and IV collagen, fibronectin and laminin. Fibronectin, laminin and types I and IV collagen are located in a network of extracellular matrix which encapsulates cells of the cytotrophoblast multilayer. The results suggest that cytotrophoblast in all layers is active in matrix biosynthesis. The pseudo-basement membrane, which links this intercellular matrix to the underlying reticular layer, contains rich deposits of fibronectin and type III collagen along with more restricted foci of laminin and type IV collagen. The reticular layer contains fibronectin, type III collagen and small amounts of type I collagen, but no laminin or type IV collagen. Type III collagen is also found in the maternal decidua. Extracellular matrix markers may be useful in defining trophoblast differentiation pathways. Possible reasons are discussed for the unusual architecture of extracellular matrix of cytotrophoblast of the chorion laeve. Cytoplasmic actin occurs in cells throughout the chorion laeve, while cytokeratin appears only in cytotrophoblast. Plasminogen also occurs throughout cytotrophoblast in pericellular locations.